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. 2018 Feb 1;8:2102. doi: 10.1038/s41598-018-20283-7

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Attractants and antagonists compete for binding at PA2652-LBD in vitro. Isothermal titration calorimetry analysis of the binding of L-malic acid to PA2652-LBD in the absence and presence of 2 or 20 mM of the antagonists, citraconic and D,L-methylsuccinic acids. Upper panel: Titration raw data for the injection of 9.6 μl aliquots of 1 mM of L-malic acid into 20 μM of protein in the absence and presence of antagonists (present both in the injector syringe and sample cell). Lower panel: Integrated, dilution heat corrected and concentration normalized peak areas fitted with the “One binding site” model of ORIGIN. The apparent binding constants are listed in Supplementary Table S2.